The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F17%3A00475665" target="_blank" >RIV/61388955:_____/17:00475665 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1038/s41598-017-02836-4" target="_blank" >http://dx.doi.org/10.1038/s41598-017-02836-4</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-017-02836-4" target="_blank" >10.1038/s41598-017-02836-4</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
Popis výsledku v původním jazyce
We have investigated the effect of lipid composition on interactions between cytochrome bo(3) and ATP-synthase, and the ATP-synthesis activity driven by proton pumping. The two proteins were labeled by fluorescent probes and co-reconstituted in large (d congruent to 100 nm) or giant (d congruent to 10 mu m) unilamellar lipid vesicles. Interactions were investigated using fluorescence correlation/cross-correlation spectroscopy and the activity was determined by measuring ATP production, driven by electron-proton transfer, as a function of time. We found that conditions that promoted direct interactions between the two proteins in the membrane (higher fraction DOPC lipids or labeling by hydrophobic molecules) correlated with an increased activity. These data indicate that the ATP-synthesis rate increases with decreasing distance between cytochrome bo3 and the ATP-synthase, and involves proton transfer along the membrane surface. The maximum distance for lateral proton transfer along the surface was found to be similar to 80 nm.
Název v anglickém jazyce
The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
Popis výsledku anglicky
We have investigated the effect of lipid composition on interactions between cytochrome bo(3) and ATP-synthase, and the ATP-synthesis activity driven by proton pumping. The two proteins were labeled by fluorescent probes and co-reconstituted in large (d congruent to 100 nm) or giant (d congruent to 10 mu m) unilamellar lipid vesicles. Interactions were investigated using fluorescence correlation/cross-correlation spectroscopy and the activity was determined by measuring ATP production, driven by electron-proton transfer, as a function of time. We found that conditions that promoted direct interactions between the two proteins in the membrane (higher fraction DOPC lipids or labeling by hydrophobic molecules) correlated with an increased activity. These data indicate that the ATP-synthesis rate increases with decreasing distance between cytochrome bo3 and the ATP-synthase, and involves proton transfer along the membrane surface. The maximum distance for lateral proton transfer along the surface was found to be similar to 80 nm.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10403 - Physical chemistry
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2017
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Scientific Reports
ISSN
2045-2322
e-ISSN
—
Svazek periodika
7
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
12
Strana od-do
—
Kód UT WoS článku
000402879200011
EID výsledku v databázi Scopus
2-s2.0-85020432705